ID D5CQY1_SIDLE Unreviewed; 577 AA.
AC D5CQY1;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Nitrite reductase (NO-forming) {ECO:0000313|EMBL:ADE11367.1};
DE EC=1.7.2.1 {ECO:0000313|EMBL:ADE11367.1};
DE Flags: Precursor;
GN OrderedLocusNames=Slit_1129 {ECO:0000313|EMBL:ADE11367.1};
OS Sideroxydans lithotrophicus (strain ES-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Sideroxydans.
OX NCBI_TaxID=580332 {ECO:0000313|EMBL:ADE11367.1, ECO:0000313|Proteomes:UP000001625};
RN [1] {ECO:0000313|EMBL:ADE11367.1, ECO:0000313|Proteomes:UP000001625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES-1 {ECO:0000313|EMBL:ADE11367.1,
RC ECO:0000313|Proteomes:UP000001625};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.;
RT "Complete sequence of Sideroxydans lithotrophicus ES-1.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001965; ADE11367.1; -; Genomic_DNA.
DR RefSeq; WP_013029265.1; NC_013959.1.
DR AlphaFoldDB; D5CQY1; -.
DR STRING; 580332.Slit_1129; -.
DR KEGG; slt:Slit_1129; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_025262_0_0_4; -.
DR OrthoDB; 5290932at2; -.
DR Proteomes; UP000001625; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IEA:UniProtKB-EC.
DR Gene3D; 2.140.10.20; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR003143; Cyt_cd1_C_sf.
DR InterPro; IPR011048; Haem_d1_sf.
DR Pfam; PF02239; Cytochrom_D1; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR SUPFAM; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Oxidoreductase {ECO:0000313|EMBL:ADE11367.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001625};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..577
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003070444"
FT DOMAIN 68..147
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 32..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 63229 MW; 439E729D73747B26 CRC64;
MKHANNRMLG LLALAALPLA LSTAFAQETA GHSSGKMETV YESSGGSPLA NSPMHQNINP
KAPSMTEAEF TRGKEIFFQR CAGCHGVLRK GATGKPLTPD ITLERGTDYL KVFINYGSPA
GMPNWGTSGE LTEAEVDLMA RYVQQEPPTP PEFGMKEMEA TWKVLVPPEK RPARQMNKLN
LKNIFSVTLR DAGKIALIDG DTKKIIKTIK TGYAVHISRI SASGRYLFVI GRDARIDLID
LWMDTPTTVA EIKIGLEARS VETSKYKGYE DKLAIAGAYW PPQFVIMDGD TLKPLKIVST
RGMTVDPQEY HPEPRVASIV ASHFKPEFLV NAKETGKIYM VNYSDLTNLK MTVIDAARFL
HDGGFDSTGR YMMVAANASN KIAVVDTKED KLAAMVDVGK TPHPGRGANF IDPKFGPVWA
TGHLGDESIS LIGTDPVKHK QNAWKVVRTI TGQGGGSLFI KTHPKSTNLW VDTPLNPDAA
LSQSVAVFDI RHLEKGYITL PIGAWAGLGE GAKRIVQPEY NAAGDEVWFS VWSAKDKESA
IVVVDDKTRT LKAVIKDPEI ITPTGKFNVY NTQHDIY
//
